Protein Crystallography and Protein Engineering


The group is involved in the crystal structure determination of Helicobacter pylori proteins relevant for bacterial infection and pathogenesis, and in the structural characterization of the calcium uniporter complex. The mechanisms of protein folding, the consequences of misfolding, and the techniques of heterologous protein expression are also investigated.


5 recent publications

  • I. Ramazzina, R. Costa, L. Cendron, R. Berni, A. Peracchi, G. Zanotti, And R. Percudani “An aminotransferase branch point connects purine catabolism to amino acid recycling” Nature Chem. Biol. (2010), 6, 801-806
  • L. Cendron, P. Berto, S. D’adamo, F. Vallese, C. Govoni, M.C. Posewitz, G.M Giacometti, P. Costantini, G. Zanotti “Crystal structure of HydF scaffold protein provides insights into [FeFe]-hydrogenase maturation” J. Biol. Chem. (2011), 286, 43944-43950
  • N. Barison, L. Cendron, V. Loconte, E.A. Proctor, N.V. Dokolian And G. Zanotti “Protein HP1028 from the human pathogen Helicobacter pylori belongs to the lipocalin’s family” Acta Cryst. D, (2013) 69, 1387-1394
  • Md M. Shaik, L. Cendron, M. Salamina, M. Ruzzene And G. Zanotti “Helicobacter pylori receptor CeuE (HP1561) modulates its nickel affinity via organic metallophores” Mol. Microbiol (2014)
  • M. Vicario, S.D Skaper, A. Negro. The small heat shock protein HspB8: role in nervous system physiology and pathology. CNS and Neurological Disorders - Drug Targets (2014)


  • University of Padua – Progetto di Ateneo
  • MIUR PRIN 2010-11
  • Futuro in ricerca 2013
  • Fidia Farmaceutici